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Database: UniProt
Entry: A0A4Z1IU99_9HELO
LinkDB: A0A4Z1IU99_9HELO
Original site: A0A4Z1IU99_9HELO 
ID   A0A4Z1IU99_9HELO        Unreviewed;       522 AA.
AC   A0A4Z1IU99;
DT   18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2019, sequence version 1.
DT   28-JAN-2026, entry version 22.
DE   RecName: Full=DAGKc domain-containing protein {ECO:0000259|PROSITE:PS50146};
GN   ORFNames=BELL_1027g00010 {ECO:0000313|EMBL:TGO64915.1};
OS   Botrytis elliptica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Botrytis.
OX   NCBI_TaxID=278938 {ECO:0000313|EMBL:TGO64915.1, ECO:0000313|Proteomes:UP000297229};
RN   [1] {ECO:0000313|EMBL:TGO64915.1, ECO:0000313|Proteomes:UP000297229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Be9601 {ECO:0000313|EMBL:TGO64915.1,
RC   ECO:0000313|Proteomes:UP000297229};
RA   Valero-Jimenez C.A., Tapia P., Veloso J., Silva-Moreno E., Staats M.,
RA   Valdes J.H., Van Kan J.A.L.;
RT   "Comparative genomics of Botrytis spp.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TGO64915.1}.
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DR   EMBL; PQXM01001025; TGO64915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4Z1IU99; -.
DR   STRING; 278938.A0A4Z1IU99; -.
DR   OrthoDB; 3853857at2759; -.
DR   Proteomes; UP000297229; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001727; F:lipid kinase activity; IEA:TreeGrafter.
DR   GO; GO:0046512; P:sphingosine biosynthetic process; IEA:TreeGrafter.
DR   Gene3D; 2.60.200.40; -; 1.
DR   Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR055916; DUF7493.
DR   InterPro; IPR050187; Lipid_Phosphate_FormReg.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR045540; YegS/DAGK_C.
DR   PANTHER; PTHR12358:SF31; ACYLGLYCEROL KINASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR12358; SPHINGOSINE KINASE; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF24321; DUF7493; 1.
DR   Pfam; PF19279; YegS_C; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000297229};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          150..290
FT                   /note="DAGKc"
FT                   /evidence="ECO:0000259|PROSITE:PS50146"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   522 AA;  57059 MW;  E9D3D91A017075BE CRC64;
     MATSPTSSNS IPPSGQTASS GSAGQFDIDN TLFVSKDVSL SLSPESLVIK GAETAKKPEK
     GAKSAGARRS VTLDASAYSE PVGASTLRAI PLRQILWAEI TETELIINYA KEISKTVLQP
     AVLKYVIEEE RDRVEAWVSR LKDRAYGKSQ QQKRVKVIIN PKSGKGQSEK IYAKDVAPIF
     DAAHLSIDVT VTKASREATD IVEKLDIEAF DVIICCSGDG LPFEVFNGLG KRKDAKRALS
     KMAIAHIPCG SGNGLHCSLH GNIRSTSIAA LSIVKGIRTP LDLISVTQGE ERHLSFLSQA
     LGIVAEFDLG TEHLRWMGGT RFVYGFVMKS LQKKIFPCDI AVKVVADDKE DIKRRYRETM
     EIGSTSEELL RENGSLEGGL PKLKYGNSSD PLPQGWEVEQ HDNLGSFYCG NMSWMGADVD
     YFPAALPNDG CMDMVTIDYS NLSRLQALQL MPAVESGKFF GLPYVNYRKV EAYRITPKNQ
     SDGYISIDGE RVPFGPFQAE VHRGLGTVLS VSGYRYETPG PK
//
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